Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa
Acta Crystallographica Section D
Volume 59, Issue 7, pages 1241–1242, July 2003
How to Cite
Karaveg, K., Liu, Z.-J., Tempel, W., Doyle, R. J., Rose, J. P. and Wang, B.-C. (2003), Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa. Acta Crystallographica D, 59: 1241–1242. doi: 10.1107/S0907444903008710
- Pseudomonas aeruginosa;
- cystic fibrosis.
Carbohydrate recognition plays a role in the pathogenesis of Pseudomonas aeruginosa, a common cause of opportunistic infection in humans. Crystals of a carbohydrate-binding protein from P. aeruginosa, lectin PA-1, have now been obtained. The crystals belong to space group I222, with unit-cell parameters a = 40.25, b = 72.30, c = 133.82 Å, and diffract to beyond 1.9 Å resolution on a rotating-anode X-ray source. Details of crystal-growth conditions, diffraction data collection and processing are reported.